Stabilisation of α-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding

Journal of Molecular Biology

Volumn 300, Issue 3, 2000, Pages 633-647

  Taddei, N ^a   Chiti, F ^b   Fiaschi, T ^a   Bucciantini, M ^a   Capanni, C ^a   Stefani, M ^a   Serrano, L ^c   Dobson, C M ^b   Ramponi, G ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Acylphosphatase; Protein folding; Transition state for folding; Trifluoroethanol; helix stabilisation

Indexed keywords

ACYLPHOSPHATASE; UREA;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS;

EID: 0034647415     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3870     Document Type: Article

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